BRENDA - Enzyme Database show
show all sequences of 1.4.99.6

Insights on the mechanism of amine oxidation catalyzed by D-arginine dehydrogenase through pH and kinetic isotope effects

Yuan, H.; Xin, Y.; Hamelberg, D.; Gadda, G.; J. Am. Chem. Soc. 133, 18957-18965 (2011)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas aeruginosa
Q9HXE3
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-leucine + phenazine methosulfate
enzyme preferentially binds the zwitterionic form of the substrate. Isomerization of the Michaelis complex yields an enzyme-substrate complex competent for flavin reduction. Amine deprotonation triggers the oxidation reaction, with cleavage of the substrate NH and CH bonds occurring in an asynchronous fashion. Tyr53, on a mobile loop covering the active site, may participate in substrate binding and facilitate flavin reduction
734025
Pseudomonas aeruginosa
? + NH3 + reduced phenazine methosulfate
-
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-leucine + phenazine methosulfate
enzyme preferentially binds the zwitterionic form of the substrate. Isomerization of the Michaelis complex yields an enzyme-substrate complex competent for flavin reduction. Amine deprotonation triggers the oxidation reaction, with cleavage of the substrate NH and CH bonds occurring in an asynchronous fashion. Tyr53, on a mobile loop covering the active site, may participate in substrate binding and facilitate flavin reduction
734025
Pseudomonas aeruginosa
? + NH3 + reduced phenazine methosulfate
-
-
-
?
Other publictions for EC 1.4.99.6
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
740089
Ouedraogo
Importance of loop L1 dynamics ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa DSM 22644
Biochemistry
56
2477-2487
2017
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2
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4
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4
4
733215
Ball
Importance of glutamate 87 and ...
Pseudomonas aeruginosa
Arch. Biochem. Biophys.
568
56-63
2015
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2
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2
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2
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8
8
724092
Akita
Efficient synthesis of D-branc ...
Ureibacillus thermosphaericus, Ureibacillus thermosphaericus A1 (NBRC 108682)
Appl. Microbiol. Biotechnol.
98
1135-1143
2014
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1
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1
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1
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1
1
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1
1
733354
Gannavaram
Mechanistic and computational ...
Pseudomonas aeruginosa
Biochemistry
53
6574-6583
2014
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2
2
724690
Oliver
Impact of D-amino acid dehydro ...
Pseudomonas aeruginosa
Can. J. Microbiol.
59
598-603
2013
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1
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5
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1
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726275
Bardaweel
E. coli histidine triad nucleo ...
Escherichia coli
PLoS ONE
6
e20897
2011
1
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6
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733330
Fu
Atomic-resolution structure of ...
Pseudomonas aeruginosa
Biochemistry
50
6292-6294
2011
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1
1
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734025
Yuan
Insights on the mechanism of a ...
Pseudomonas aeruginosa
J. Am. Chem. Soc.
133
18957-18965
2011
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748083
He
Regulation and characterizati ...
Pseudomonas aeruginosa
J. Bacteriol.
193
2107-2115
2011
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1
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9
1
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3
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9
1
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1
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1
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3
3
1
9
9
695533
Tanigawa
D-Amino acid dehydrogenase fro ...
Helicobacter pylori, Helicobacter pylori NCTC 11637
Amino Acids
38
247-255
2010
-
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1
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5
2
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1
2
2
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2
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1
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8
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16
1
1
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1
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1
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733326
Fu
Conformational changes and sub ...
Pseudomonas aeruginosa
Biochemistry
49
8535-8545
2010
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1
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7
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2
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7
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7
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7
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7
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7
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733327
Yuan
Steady-state kinetic mechanism ...
Pseudomonas aeruginosa
Biochemistry
49
9542-9550
2010
-
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2
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2
705545
Ye
Heterologous expression of the ...
Helicobacter pylori NCTC 11637 = CCUG 17874 = ATCC 43504
Microbiol. Res.
165
268-275
2009
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1
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4
2
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705583
Li
Regulation of the dauBAR Opero ...
Pseudomonas aeruginosa
Microbiology
156
60-71
2009
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1
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2
7
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2
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1
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7
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1
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7
706547
Li
Arginine racemization by coupl ...
Pseudomonas aeruginosa
Proc. Natl. Acad. Sci. USA
106
906-911
2009
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394974
Tsukada
-
D-Amino acid dehydrogenase (Ps ...
Pseudomonas fluorescens
Methods Enzymol.
17B
623-624
1971
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1
3
4
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1
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2
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30
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1
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3
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30
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394975
Tsukada
D-Amino acid dehydrogenases of ...
Pseudomonas fluorescens
J. Biol. Chem.
241
4522-4528
1966
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